1ow5

NMR structure of the Saccharomyces cerevisiae SAM (Sterile Alpha Motif) domainNMR structure of the Saccharomyces cerevisiae SAM (Sterile Alpha Motif) domain

Structural highlights

1ow5 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STE11_YEAST Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it phosphorylates the STE7 protein kinase which itself, phosphorylates the FUS3 and or KSS1 kinases.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Ste11 is a MAPKKK from Saccharomyces cerevisiae that helps mediate the response to mating pheromone and the ability to thrive in high-salt environments. These diverse functions are facilitated by a direct interaction between the SAM domain of Ste11 with the SAM domain of its regulatory partner, Ste50. We have solved the NMR structure of the Ste11 SAM domain (PDB 1OW5), which reveals a compact, five alpha-helix bundle and a high degree of structural similarity to the Polyhomeotic SAM domain. The combined study of Ste11 SAM rotational correlation times and crosslinking to Ste50-SAM has suggested a mode through which Ste11-SAM oligomerizes and selectively associates with Ste50-SAM. To probe homotypic and heterotypic interations, Ste11-SAM variants each containing a substitution of a surface-exposed hydrophobic residue were constructed. An I59R variant of Ste11-SAM, disrupted binding to Ste50-SAM in vitro. Yeast expressing full-length Ste11-I59R could neither respond to mating pheromone nor thrive in high salt media-demonstrating that the interaction between Ste11 and Ste50 SAM domains is a prerequisite for key signal transduction events.

The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50.,Kwan JJ, Warner N, Pawson T, Donaldson LW J Mol Biol. 2004 Sep 10;342(2):681-93. PMID:15327964^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cairns BR, Ramer SW, Kornberg RD. Order of action of components in the yeast pheromone response pathway revealed with a dominant allele of the STE11 kinase and the multiple phosphorylation of the STE7 kinase. Genes Dev. 1992 Jul;6(7):1305-18. PMID:1628833
↑ Zarrinpar A, Bhattacharyya RP, Nittler MP, Lim WA. Sho1 and Pbs2 act as coscaffolds linking components in the yeast high osmolarity MAP kinase pathway. Mol Cell. 2004 Jun 18;14(6):825-32. PMID:15200959 doi:http://dx.doi.org/10.1016/j.molcel.2004.06.011
↑ Kwan JJ, Warner N, Pawson T, Donaldson LW. The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50. J Mol Biol. 2004 Sep 10;342(2):681-93. PMID:15327964 doi:10.1016/j.jmb.2004.06.064

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OCA

[1] Cairns BR, Ramer SW, Kornberg RD. Order of action of components in the yeast pheromone response pathway revealed with a dominant allele of the STE11 kinase and the multiple phosphorylation of the STE7 kinase. Genes Dev. 1992 Jul;6(7):1305-18. PMID:1628833

[2] Zarrinpar A, Bhattacharyya RP, Nittler MP, Lim WA. Sho1 and Pbs2 act as coscaffolds linking components in the yeast high osmolarity MAP kinase pathway. Mol Cell. 2004 Jun 18;14(6):825-32. PMID:15200959 doi:http://dx.doi.org/10.1016/j.molcel.2004.06.011

[3] Kwan JJ, Warner N, Pawson T, Donaldson LW. The solution structure of the S.cerevisiae Ste11 MAPKKK SAM domain and its partnership with Ste50. J Mol Biol. 2004 Sep 10;342(2):681-93. PMID:15327964 doi:10.1016/j.jmb.2004.06.064

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